scholarly journals Acute Metabolic Response in Adults to Toddler Milk Formulas with Alternating Higher and Lower Protein and Fat Contents, a Randomized Cross-Over Trial

Nutrients ◽  
2021 ◽  
Vol 13 (9) ◽  
pp. 3022
Author(s):  
Emily Newton-Tanzer ◽  
Hans Demmelmair ◽  
Jeannie Horak ◽  
Lesca Holdt ◽  
Berthold Koletzko ◽  
...  
Keyword(s):  
Amino Acids ◽  
Protein Intake ◽  
Metabolic Response ◽  
Plasma Concentrations ◽  
Postprandial Metabolism ◽  
Postprandial Phase ◽  
Lower Protein ◽  
Branched Chain ◽  
Underlying Mechanisms ◽  
Time Specific

Protein intake in early life influences metabolism, weight gain, and later obesity risk. As such, a better understanding of the effects of protein intake on the postprandial metabolism and its dynamics over time may elucidate underlying mechanisms. In a randomized crossover study, we observed fasted adults who consumed two isocaloric toddler milk formulas concentrated as meals of 480 kcal with 67 g of carbohydrates 30 g (HP) or 7 g (LP) protein, and 10 g or 20 g fat, respectively. Anthropometry and body plethysmography were assessed, and blood samples collected at baseline and over five hours. Time-specific concentrations, areas under concentration curves (AUC), and maximum values of metabolites were compared by paired t-tests to examine the effects of protein content of toddler milks on postprandial plasma concentrations of insulin, glucose, branched-chain amino acids (BCAA), urea and triglycerides. Twenty-seven men and women aged 26.7 ± 5.0 years (BMI: 22.2 ± 2.5 kg/m2) (mean ± SD) participated. BCAA AUC, and Cmax values were significantly higher with HP than LP (144,765 ± 21,221 vs. 97,089 ± 14,650 µmol min/L, p < 0.001; 656 ± 120 vs. 407 ± 66 µmol/L, p < 0.001), as were insulin AUC and Cmax values (6674 ± 3013 vs. 5600 ± 2423 µmol min/L, p = 0.005; 71 ± 37 vs. 55 ± 28 µmol /L, p = 0.001). Higher glucose, urea, and triglyceride concentrations occurred in the late postprandial phase (≥180 min) with HP. In conclusion, we noted that higher milk protein intake induces increased postprandial BCAA concentrations for at least 5 h and led to higher initial insulin secretion. Gluconeogenesis due to an influx of amino acids and their degradation after HP meal might explain the late effects of protein intake on glucose and insulin.

scholarly journals Natural Isotope Abundances of Carbon and Nitrogen in Tissue Proteins and Amino Acids as Biomarkers of the Decreased Carbohydrate Oxidation and Increased Amino Acid Oxidation Induced by Caloric Restriction under a Maintained Protein Intake in Obese Rats

Nutrients ◽  
2019 ◽  
Vol 11 (5) ◽  
pp. 1087 ◽  
Author(s):  
Jean-François Huneau ◽  
Olivier L. Mantha ◽  
Dominique Hermier ◽  
Véronique Mathé ◽  
Guillaume Galmiche ◽  
...  
Keyword(s):  
Amino Acids ◽  
Caloric Restriction ◽  
Protein Intake ◽  
Skeletal Muscles ◽  
Acid Oxidation ◽  
Protein Mass ◽  
Obese Rats ◽  
Lower Protein ◽  
Underlying Mechanisms ◽  
Δ15n And Δ13c

A growing body of evidence supports a role for tissue-to-diet 15N and 13C discrimination factors (Δ15N and Δ13C), as biomarkers of metabolic adaptations to nutritional stress, but the underlying mechanisms remain poorly understood. In obese rats fed ad libitum or subjected to gradual caloric restriction (CR), under a maintained protein intake, we measured Δ15N and Δ13C levels in tissue proteins and their constitutive amino acids (AA) and the expression of enzymes involved in the AA metabolism. CR was found to lower protein mass in the intestine, liver, heart and, to a lesser extent, some skeletal muscles. This was accompanied by Δ15N increases in urine and the protein of the liver and plasma, but Δ15N decreases in the proteins of the heart and the skeletal muscles, alongside Δ13C decreases in all tissue proteins. In Lys, Δ15N levels rose in the plasma, intestine, and some muscles, but fell in the heart, while in Ala, and to a lesser extent Glx and Asx, Δ13C levels fell in all these tissues. In the liver, CR was associated with an increase in the expression of genes involved in AA oxidation. During CR, the parallel rises of Δ15N in urine, liver, and plasma proteins reflected an increased AA catabolism occurring at the level of the liver metabolic branch point, while Δ15N decreases in cardiac and skeletal muscle proteins indicated increased protein and AA catabolism in these tissues. Thus, an increased protein and AA catabolism results in opposite Δ15N effects in splanchnic and muscular tissues. In addition, the Δ13C decrease in all tissue proteins, reflects a reduction in carbohydrate (CHO) oxidation and routing towards non-indispensable AA, to achieve fuel economy.

scholarly journals Reduced plasma concentration of branched-chain amino acids in sarcopenic older subjects: a cross-sectional study

2018 ◽  
Vol 120 (4) ◽  
pp. 445-453 ◽  
Author(s):  
Inger Ottestad ◽  
Stine M. Ulven ◽  
Linn K. L. Øyri ◽  
Kristin S. Sandvei ◽  
Gyrd O. Gjevestad ◽  
...  
Keyword(s):  
Amino Acids ◽  
Plasma Concentration ◽  
Protein Intake ◽  
Plasma Concentrations ◽  
Cross Sectional Study ◽  
Branched Chain Amino Acids ◽  
Sectional Study ◽  
Cross Sectional ◽  
Fasting Plasma ◽  
Branched Chain

AbstractBranched-chain amino acids (BCAA) are essential amino acids that are necessary for muscle mass maintenance. Little is known about the plasma concentrations of BCAA and the protein intake in relation to sarcopenia. We aimed to compare the non-fasting plasma concentrations of the BCAA and the dietary protein intake between sarcopenic and non-sarcopenic older adults. Norwegian older home-dwelling adults (≥70 years) were invited to a cross-sectional study with no other exclusion criteria than age. Sarcopenic subjects were defined by the diagnostic criteria by the European Working Group on Sarcopenia in Older People. Non-fasting plasma concentrations of eight amino acids were quantified using NMR spectroscopy. Protein intake was assessed using 2×24-h dietary recalls. In this study, ninety out of 417 subjects (22 %) were sarcopenic, and more women (32 %) than men (11 %) were sarcopenic (P<0·0001). Sex-adjusted non-fasting plasma concentrations of leucine and isoleucine, and the absolute intake of protein (g/d), were significantly lower among the sarcopenic subjects, when compared with non-sarcopenic subjects (P=0·003, P=0·026 and P=0·003, respectively). A similar protein intake was observed in the two groups when adjusted for body weight (BW) and sex (1·1 g protein/kg BW per d; P=0·50). We show that sarcopenia is associated with reduced non-fasting plasma concentration of the BCAA leucine and isoleucine, and lower absolute intake of protein. More studies are needed to clarify the clinical relevance of these findings, related to maintenance of muscle mass and prevention of sarcopenia.

Response of hepatic proteins to the lowering of habitual dietary protein to the recommended safe level of intake

2004 ◽  
Vol 287 (2) ◽  
pp. E327-E330 ◽  
Author(s):  
Paul R. Afolabi ◽  
Farook Jahoor ◽  
Neil R. Gibson ◽  
Alan A. Jackson
Keyword(s):  
Protein Intake ◽  
Acute Phase Proteins ◽  
Metabolic Response ◽  
Plasma Concentrations ◽  
Nutrient Transport ◽  
Apolipoprotein A1 ◽  
Retinol Binding Protein ◽  
Safe Level ◽  
Lower Protein ◽  
Hepatic Proteins

The plasma concentrations of albumin, HDL apolipoprotein A1 (apoA1), retinol-binding protein (RBP), transthyretin (TTR), haptoglobulin, and fibrinogen were measured, and a stable isotope infusion protocol was used to determine the fractional and absolute synthesis rates of RBP, TTR, and fibrinogen in 12 young adults on three occasions during a reduction of their habitual protein intake from 1.13 to 0.75 g·kg−1·day−1 for 10 days. This study was performed to determine whether healthy adults could maintain the rates of synthesis of selected nutrient transport and positive acute-phase proteins when consuming a protein intake of 0.75 g·kg−1·day−1. During the lower protein intake, the plasma concentration of all the proteins, other than HDL-apoA1, remained unchanged. HDL-apoA1 concentration was significantly reduced ( P < 0.05) after 3 days of the lower protein intake, but not at 10 days. The rates of synthesis of RBP and TTR declined significantly ( P < 0.05), whereas the rate of synthesis of fibrinogen remained unchanged. The results indicate that, when normal adults consume the recommended safe level of protein, 0.75 g·kg−1·day−1, there is a slower rate of turnover of nutrient transport proteins than on their habitual diet. Hence, healthy individuals consuming this amount of protein may be less able to mount an adequate metabolic response to a stressful stimulus.

Effect of protein intake on weight gain and plasma amino acid levels in uremic rats

1976 ◽  
Vol 230 (5) ◽  
pp. 1455-1459 ◽  
Author(s):  
M Wang ◽  
I Vyhmeister ◽  
JD Kopple ◽  
ME Swendseid
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Protein Intake ◽  
Plasma Concentrations ◽  
Plasma Amino Acid ◽  
Uremic Patient ◽  
Lower Protein ◽  
Similar Weight ◽  
Amino Acid Levels ◽  
And Control

Chronically uremic rats weighing approximately 180-200 g and sham-operated controls of similar weight were pair fed diets containing 5, 15 or 23% protein for 10-12 wk. At each level of protein intake, uremic animals gained less weight and had lower protein efficiency ratios than controls. In addition, certain plasma amino acid levels were altered in the uremic animals. These included tyrosine and the tyrosine/phenylalanine ratio, which were decreased, and citrulline, glycine, and the methylhistidines, which were increased. In both uremic and control rats, plasma concentrations of certain amino acids, primarily nonessential ones, varied inversely with protein intake; with the 5% protein diet, the ratio of essential to nonessential amino acids was significantly reduced. These observations indicate that both uremia and reduced protein intake may affect growth and amino acid metabolism in rats with chronic renal failure. The finding that uremic rats utilize protein less efficiently may indicate that marked reductions in protein intake may be particularly hazardous to the nutritional status of the uremic patient.

scholarly journals Severe anemia in patients with Propionic acidemia is associated with branched-chain amino acid imbalance

2021 ◽  
Vol 16 (1) ◽  
Author(s):  
Sinziana Stanescu ◽  
Amaya Belanger-Quintana ◽  
Borja Manuel Fernandez-Felix ◽  
Francisco Arrieta ◽  
Victor Quintero ◽  
...  
Keyword(s):  
Amino Acids ◽  
Food Consumption ◽  
Protein Intake ◽  
Propionic Acidemia ◽  
Study Data ◽  
Metabolic Decompensation ◽  
Severe Anemia ◽  
Medical Food ◽  
Natural Protein ◽  
Branched Chain

Abstract Background Propionic acidemia (PA), an inborn error of metabolism, is caused by a deficiency in propionyl-CoA carboxylase. Patients have to follow a diet restricted in the propiogenic amino acids isoleucine (Ile), valine (Val), methionine (Met) and threonine (Thr); proper adherence can prevent and treat acute decompensation and increase life expectancy. However, chronic complications occur in several organs even though metabolic control may be largely maintained. Bone marrow aplasia and anemia are among the more common. Materials and methods In this retrospective study, data for patients with PA being monitored at the Hospital Ramón y Cajal (Madrid, Spain) (n = 10) in the past 10 years were examined to statistically detect relationships between persistent severe anemia outside of metabolic decompensation episodes and dietary practices such as natural protein intake and medical food consumption (special mixture of precursor-free amino acids) along with plasma levels of branched-chain amino acids (BCAA). High ferritin levels were deemed to indicate that a patient had received repeated transfusions for persistent anemia since data on hemoglobin levels at the moment of transfusion were not always passed on by the attending centers. Results Three patients had severe, persistent anemia that required repeated blood transfusions. Higher medical food consumption and plasma Leu levels were associated with iron overload. Notably, natural protein intake and plasma Val were negatively correlated with ferritin levels. We also observed an inverse relationship between plasma Val/Leu and Ile/Leu ratios and ferritin. Conclusion The present results suggest that severe anemia in patients with PA might be associated with low natural protein intake and BCAA imbalance.

scholarly journals Association between plasma concentrations of branched-chain amino acids and adipokines in Japanese adults without diabetes

2018 ◽  
Vol 8 (1) ◽  
Author(s):  
Ryoko Katagiri ◽  
Atsushi Goto ◽  
Sanjeev Budhathoki ◽  
Taiki Yamaji ◽  
Hiroshi Yamamoto ◽  
...  
Keyword(s):  
Amino Acids ◽  
Plasma Concentrations ◽  
Branched Chain Amino Acids ◽  
Japanese Adults ◽  
Branched Chain

scholarly journals Metabolic consequences of methylenecyclopropylglycine poisoning in rats

1991 ◽  
Vol 274 (2) ◽  
pp. 395-400 ◽  
Author(s):  
K Melde ◽  
S Jackson ◽  
K Bartlett ◽  
H S A Sherratt ◽  
S Ghisla
Keyword(s):  
Amino Acids ◽  
Ketone Bodies ◽  
Blood Glucose Concentration ◽  
Plasma Concentrations ◽  
Liver Mitochondria ◽  
Branched Chain Amino Acids ◽  
Oxidation Products ◽  
Rat Liver Mitochondria ◽  
Toxic Metabolite ◽  
Branched Chain

We describe the effects of methylenecyclopropylglycine in fasted rats. A 75% decrease in the blood glucose concentration and an increase of lactate and pyruvate were observed 6 h after administration of 100 mg of this amino acid/kg. By contrast with the effects reported for hypoglycin [Williamson & Wilson (1965) Biochem. J. 94, 19c-21c], the plasma concentrations of ketone bodies decreased after administration of methylenecyclopropylglycine and the concentrations of branched-chain amino acids in the plasma were increased 6-fold. The oxidation of decanoylcarnitine or of palmitate was nearly completely inhibited in rat liver mitochondria from methylenecyclopropylglycine-poisoned rats. The activities of acetoacetyl-CoA and of 3-oxoacyl-CoA thiolase were decreased to 25% and less than 10% of the controls. There was a pronounced aciduria, due to the excretion of dicarboxylic acids and of oxidation products of branched-chain amino acids. The accumulation of the toxic metabolite methylenecyclopropylformyl-CoA in the mitochondrial matrix was detected after administration of methylenecyclopropylglycine. Similarly we confirmed experimentally that methylenecyclopropylacetyl-CoA accumulates in mitochondria incubated with methylenecyclopropylpyruvate.

Amino acid metabolism in the Zucker diabetic fatty rat: effects of insulin resistance and of type 2 diabetes

2004 ◽  
Vol 82 (7) ◽  
pp. 506-514 ◽  
Author(s):  
Enoka P Wijekoon ◽  
Craig Skinner ◽  
Margaret E Brosnan ◽  
John T Brosnan
Keyword(s):  
Insulin Resistance ◽  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Metabolism ◽  
Acid Metabolism ◽  
Plasma Concentrations ◽  
Branched Chain Amino Acids ◽  
Insulin Resistant ◽  
Branched Chain

We investigated amino acid metabolism in the Zucker diabetic fatty (ZDF Gmi fa/fa) rat during the prediabetic insulin-resistant stage and the frank type 2 diabetic stage. Amino acids were measured in plasma, liver, and skeletal muscle, and the ratios of plasma/liver and plasma/skeletal muscle were calculated. At the insulin-resistant stage, the plasma concentrations of the gluconeogenic amino acids aspartate, serine, glutamine, glycine, and histidine were decreased in the ZDF Gmi fa/fa rats, whereas taurine, α-aminoadipic acid, methionine, phenylalanine, tryptophan, and the 3 branched-chain amino acids were significantly increased. At the diabetic stage, a larger number of gluconeogenic amino acids had decreased plasma concentrations. The 3 branched-chain amino acids had elevated plasma concentrations. In the liver and the skeletal muscles, concentrations of many of the gluconeogenic amino acids were lower at both stages, whereas the levels of 1 or all of the branched-chain amino acids were elevated. These changes in amino acid concentrations are similar to changes seen in type 1 diabetes. It is evident that insulin resistance alone is capable of bringing about many of the changes in amino acid metabolism observed in type 2 diabetes.Key words: plasma amino acids, liver amino acids, muscle amino acids, gluconeogenesis.

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